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Kiwifruit Enzyme: a New Plant Coagulant for the Development of Cottage Cheese

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Kiwifruit Enzyme: a New Plant Coagulant for the Development of Cottage Cheese International Journal of Food Science and Nutrition International Journal of Food Science and Nutrition ISSN: 2455-4898 Impact Factor: RJIF 5.14 www.foodsciencejournal.com Volume 3; Issue 1; January 2018; Page No. 12-19 Kiwifruit enzyme: A new plant coagulant for the development of cottage cheese * Swati Sharma, Devina Vaidya Department of Food Science and Technology, YSP University of Horticulture and Forestry, Nauni, Solan, Himachal Pradesh, India Abstract In the present work, extraction of kiwifruit enzyme, partial purification, characterization, optimization of enzyme concentration, quality of cottage cheese prepared and their comparative study with animal rennet was studied. In the experiment, first enzyme was extracted at various stages of maturity followed by partial purification, characterization and optimization of enzyme concentration was done. Results showed that kiwifruit enzyme has maximum enzyme activity at immature stage and partial purification with ammonium sulphate precipitation method at 40-60 per cent shows the highest yield. Characterization of enzyme through Response Surface Methodology (RSM) shows that enzyme was stable at pH (8) and temperature (450C). The quality of cottage cheese prepared with kiwifruit enzyme was comparable to the rennet cottage cheese. Therefore, it was finally concluded that animal origin rennet can be completely or effectively replaced by employing plant kiwifruit partially purified enzyme at the rate of 0.5 per cent for cottage cheese production. Keywords: kiwifruit enzyme, characterization, partial purification, cottage cheese, rennet 1. Introduction 2. Materials and methods Kiwifruit (Actinidia deliciosa) is native to Southern China [10]. 2.1 Procurement of raw material Kiwifruit is very popular in human diet due to its pleasant The raw material i.e. kiwifruit (Actinidia deliciosa) was taste and high content of vitamin C, minerals (potassium, procured from Kiwifruit Orchard, Department of Fruit phosphorus, iron) and low calorific value. Kiwifruits are good Science, milk from Dairy Farm, Department of Silviculture sources of folate, potassium and contain large amounts of and Agroforestry, YSP University of Horticulture and vitamin E in the seeds. Moreover, kiwifruit juice is known to Forestry, Nauni-Solan (India), while rennet was procured from contain highly active proteolytic enzymes [14]. Enzymes are Guru Angad Dev Veteniary and Animal Sciences University, widely used as technological aids in several food processes. Ludhiana, Punjab (India). However other materials used for Proteolytic enzymes are multifunctional class of enzymes [22]. producing cottage cheese viz. starter culture and salt were Henceforth kiwifruit enzyme as a proteolytic enzyme can be obtained from the local market of Nauni-Solan, Himachal used in food industry as milk clotting enzyme. Kiwifruit Pradesh (India). enzyme has the ability to form milk clots so that the enzyme is fully compatible with conditions used in cheese manufacture 2.2 Estimation of soluble protein in kiwifruit (optimum activity at 40-42oC, mildly acidic pH values). Protein concentration in kiwifruit was determined using Analysis of products produced by hydrolysis by using procedure followed by Lowry [16]. actinidin showed that the preferred substrate for this enzyme is β-casein, followed by k-casein, which is hydrolysed into a 2.3 Extraction of crude enzyme small number of larger peptides [18]. Milk coagulation is a The procedure followed by Thimmaiah [31] was employed for basic step in cheese manufacturing and is most commonly extraction of crude enzyme from kiwifruit. First the kiwifruit achieved by addition of chymosin (rennet), milk clotting tissues were homogenized in pestle-mortar with phosphate enzyme preparation obtained from the stomach contents of the buffer (pH 8.0) under cool condition (0-50C) and extract was unweaned calf [19]. The worldwide increase in cheese centrifuged at 10,000 rpm for 10 min in refrigerated production, alongside with the reduced supply of calf rennet centrifuge. The supernatant was labeled as “Crude enzyme”. and higher prices, have led to an increase in the demand for alternative sources of milk coagulants [6]. In addition, the use 2.4 Partial purification of enzyme of animal rennet has consumer constraints due to religious The procedure followed by Sadasivam and Manickam [28] was reasons (e.g. Judaism and Islam), diet (vegetarianism), or bans employed for partial purification of enzyme extracted from on genetically engineered food [27]. For these reasons, enzymes kiwifruit. First partial purification of enzyme was done by extracted from plants have become a subject of growing using ammonium sulphate fractionation method as mentioned interest in dairy technology. Henceforth, present study was above. The crude extract of kiwifruit was precipitated by planned to assess the effect of kiwifruit enzyme on quality ammonium sulphate using different concentrations (0-90 per attributes of cottage cheese as potential vegetable coagulant to cent). Precipitation was carried out at 0-50C and the replace the animal origin rennet. precipitate was recovered by centrifugation. The supernatant 12 International Journal of Food Science and Nutrition was discarded and the sediment from each concentration was version 7.0 (Stat Ease, Inc, Minneapolis, USA). The details of dissolved in phosphate buffer solution (pH 8.0) and dialyzed experimental design plan for characterization of enzyme are over night against the same buffer. The dialyzed enzyme was given in Table 2. used for further studies. Observations recorded dring partial purification are- Table 1: Range of values for the RSM Variables -1 0 +1 [4] 2.4.1 Specific activity pH 4 8 12 Specific activity was calculated by dividing the total enzyme Temperature (0C) 30 45 60 activity with total protein. Incubation Time (min) 10 20 30 2.5.1 Experimental design and equation modelling Second-order experimental design, i.e. Central Composite Design (CCD) with three factors at three levels was employed 2.4.2 Fold purification [4] to investigate the first and higher-order main effects of each Fold purification was calculated by dividing the specific factor as well as interactions among them. The design activity of partially purified enzyme with specific activity of involved eight center design points with ‘α’ value being ± 2. crude enzyme. The three coded levels investigated in the current study were - 1, 0, and 1 as shown in table. The enzyme assay conditions were optimized on the basis of highest enzyme activity. The experimental results obtained by the characterization of [4] enzyme were applied to obtain the regression models. Based 2.4.3 Per cent yield / Recovery of enzyme on experimental design (Table 1), the cubic model could be Percent yield / Recovery was calculated by dividing the total fitted in case the lacks of fit of the quadratic or linear models enzyme activity of partially purified enzyme with total activity were statistically significant (p<0.05), Where Y , evaluated of crude enzyme. i response; b terms were coefficients estimated by the least square 2.5 Characterization of enzyme Response Surface Methodology (RSM) was used for the characterization of the enzyme by keeping the effects of pH, method; x terms were dependent variables [9]. Quality of the temperature, time of incubation as independent variables and models fitness was evaluated by ANOVA, in which the enzyme activity as a dependent variable. As per the design repetition supplied the freedom degree to obtain the pure treatments chosen were shown in Table 1. The different error. Calculations and graphics were performed by opstat. combinations were made as per the expert RSM design This was used at the beginning of this study. Table 2: Experimental plan of characterization of enzyme as per the design Treatments Factor 1 A:pH Factor 2 B:Temp (0C) Factor 3 C: Time of incubation (min) T1 8.00 45.00 20.00 T2 4.00 30.00 10.00 T3 1.27 45.00 20.00 T4 8.00 45.00 20.00 T5 8.00 45.00 20.00 T6 12.00 60.00 30.00 T7 8.00 45.00 20.00 T8 8.00 45.00 36.82 T9 12.00 30.00 10.00 T10 8.00 70.23 20.00 T11 4.00 30.00 30.00 T12 12.00 60.00 10.00 T13 8.00 45.00 20.00 T14 4.00 60.00 30.00 T15 4.00 60.00 10.00 T16 14.73 45.00 20.00 T17 8.00 45.00 20.00 T18 12.00 30.00 30.00 T19 8.00 19.77 20.00 T20 8.00 45.00 3.18 13 International Journal of Food Science and Nutrition 2.6 Enzyme assay 2.9.2 Proximate analysis The procedure followed by Thimmaiah [31] was employed for The moisture content, crude protein, crude fat and ash content assessment of enzyme assay with slight modifications. For were determined in triplicates following methods of AOAC [2]. this, one ml of reaction mixture containing 1 per cent casein in 1 ml of 0.05 M phosphate buffer, pH 8.0 and 1 ml of enzyme 2.9.3 Calcium content was incubated at 45°C for 20 min. After 2hr, the reaction was The AOAC method [2] was followed for estimation of calcium stopped by adding 2ml of cold 10 per cent trichloroacetic acid content. For that one gram of cheese sample digested in 20 ml (TCA) and for blank, immediately after incubation reaction concentrated sulphuric acid till 3-4 ml extract was remained was stopped with 10 per cent TCA. After 2 hour, the culture after that it was diluted with distilled water to make 100 ml filtrate was centrifuged at 10,000 rpm for 10 min in final volume. Then calcium content was estimated with flame refrigerated high speed research centrifuge (Model TC 4100 photometer with standard procedure. F/RC 4100 F) to remove the precipitate and absorbance of the supernatant was read spectrophotometrically at 660 nm. 2.9.4 Total carbohydrates Enzyme activity was calculated by measuring mg of tyrosine The total carbohydrate content as per cent dry weight basis equivalent released and compared with the standard.
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